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Science 16 February 1996:
Vol. 271. no. 5251, pp. 981 - 983
DOI: 10.1126/science.271.5251.981
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Reports

Role of Rho in Chemoattractant-Activated Leukocyte Adhesion Through Integrins

Carlo Laudanna (1),  James J. Campbell,  Eugene C. Butcher

Heterotrimeric guanine nucleotide binding protein (G protein)-linked receptors of the chemoattractant subfamily can trigger adhesion through leukocyte integrins, and in this role they are thought to regulate immune cell-cell interactions and trafficking. In lymphoid cells transfected with formyl peptide or interleukin-8 receptors, agonist stimulation activated nucleotide exchange on the small guanosine triphosphate-binding protein RhoA in seconds. Inactivation of Rho by C3 transferase exoenzyme blocked agonist-induced lymphocyte alpha4beta1 adhesion to vascular cell adhesion molecule-1 and neutrophil beta2 integrin adhesion to fibrinogen. These findings suggest that Rho participates in signaling from chemoattractant receptors to trigger rapid adhesion in leukocytes.


Laboratory of Immunology and Vascular Biology, Department of Pathology, and Digestive Disease Center, Stanford University, Stanford, CA 94305, USA, and Center for Molecular Biology and Medicine, Veterans Affairs Health Care System, Palo Alto, CA 94304, USA.
(1) To whom correspondence should be addressed.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)